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A more recent version of this article appeared on February 1, 2007 Originally published as MBC in Press, 10.1091/mbc.E06-07-0612 on November 29, 2006
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Submitted on July 19, 2006
Revised on November 1, 2006
Accepted on November 21, 2006
Life Sciences Institute, and Departments of Molecular, Cellular and Developmental Biology and Biological Chemistry, University of Michigan, Ann Arbor, MI 48109
Monitoring Editor: Suresh Subramani
Autophagy is a catabolic pathway for the degradation of cytosolic proteins or organelles and is conserved among all eukaryotic cells. The hallmark of autophagy is the formation of double-membrane cytosolic vesicles, termed autophagosomes, which sequester cytoplasm; however, the mechanism of vesicle formation and the membrane source remain unclear. In the yeast S. cerevisiae, selective autophagy mediates the delivery of specific cargos to the vacuole, the analog of the mammalian lysosome. The transmembrane protein Atg9 cycles between the mitochondria and the pre-autophagosomal structure, which is the site of autophagosome biogenesis. Atg9 is thought to mediate the delivery of membrane to the forming autophagosome. Here, we characterize a second transmembrane protein Atg27 that is required for specific autophagy in yeast. Atg27 is required for Atg9 cycling, and shuttles between the pre-autophagosomal structure, mitochondria and the Golgi complex. These data support a hypothesis that multiple membrane sources supply the lipids needed for autophagosome formation.
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